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Information on EC 2.3.1.B43 - protein-lysine desuccinylase (NAD+)
for references in articles please use BRENDA:EC2.3.1.B43preliminary BRENDA-supplied EC number
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EC Tree
2.3.1.B43 protein-lysine desuccinylase (NAD+)Specify your search results
Word Map
- 2.3.1.B43
- sirtuins
- sirt3
-
deacetylation
- deacetylases
-
desuccinylation
-
malonylation
-
nad-dependent
-
sirt1-7
-
glutarylation
- medicine
- drug development
- diagnostics
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Reaction Schemes
Synonyms
CobB, CobB Sir2 protein, histone desuccinylase, hSIRT5, hSIRT6, lysine desuccinylase, mitochondrial NAD+-dependent lysine deacylase, NAD+ dependent deacetylase, NAD+-dependent protein deacetylase, NAD+-dependent protein deacylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CobB
lysine desuccinylase
NAD+-dependent protein deacetylase
nicotinamide adenine dinucleotide-dependent protein deacetylase
SIRT5
SIRT5iso1
SIRT5iso2
sirtuin 5
sirtuin 5 deacylase
sirtuin deacylase
SIRT5
-
SIRT5
SIRT5 isoforms (i.e., SIRT5iso1 and SIRT5iso2) are encoded by the human SIRT5 gene. Their C-termini slightly differ from each other. Although both isoforms contain cleavable mitochondrial targeting signals at their N-termini, it is found that the cleaved SIRT5iso2 is localized mainly in mitochondria, whereas the cleaved SIRT5iso1 is localized in both mitochondria and cytoplasm
SIRT5iso1
SIRT5 isoforms (i.e., SIRT5iso1 and SIRT5iso2) are encoded by the human SIRT5 gene. Their C-termini slightly differ from each other. Although both isoforms contain cleavable mitochondrial targeting signals at their N-termini, it is found that the cleaved SIRT5iso2 is localized mainly in mitochondria, whereas the cleaved SIRT5iso1 is localized in both mitochondria and cytoplasm
SIRT5iso2
SIRT5 isoforms (i.e., SIRT5iso1 and SIRT5iso2) are encoded by the human SIRT5 gene. Their C-termini slightly differ from each other. Although both isoforms contain cleavable mitochondrial targeting signals at their N-termini, it is found that the cleaved SIRT5iso2 is localized mainly in mitochondria, whereas the cleaved SIRT5iso1 is localized in both mitochondria and cytoplasm. SIRT5iso2 is a primate-specific isoform
sirtuin 5
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NAD+ + [protein]-N6-acetyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [protein]-N6-succinyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
NAD+ + [protein]-N6-acetyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
crystallographic evidence is provided that 2'-O-acetyl ADP-ribose is a final product in the Sir2 reaction. A revised mechanism for catalysis based on the structural and functional characterization of Sir2 mutants is proposed. In this mechanism, the activation of the 2'-OH of nicotinamide ribose by His-116 is essential for the hydrolysis of the acetyl groups from N-acetyl lysine. The conserved Ser-24 and Asp-101 participate in the stabilization of local structure for NAD binding rather than direct involvement in catalysis
NAD+ + [protein]-N6-acetyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
NAD+ + [protein]-N6-succinyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
most efficient at catalyzing desuccinylation, medium-chain deacylation (octanoyl-, decanoyl-, dodecanoyl-) is catalyzed with lower activity
NAD+ + [protein]-N6-succinyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD+ + Ac-(N6-methylmalonyl)Lys-(7-amido-4-methylcoumarin)
nicotinamide + Ac-Lys-7-amido-4-methylcoumarin + 2'-O-methylmalonyl-ADP-ribose
-
-
-
?
NAD+ + Ac-(N6-succinyl)Lys-7-amido-4-methylcoumarin
nicotinamide + Ac-Lys-7-amido-4-methylcoumarin + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + Ac-Leu-Gly-(N6-malonyl)Lys-7-amido-4-methylcoumarin
nicotinamide + Ac-Leu-Gly-Lys-7-amido-4-methylcoumarin + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + Ac-Leu-Gly-(N6-succinyl)Lys-7-amido-4-methylcoumarin
nicotinamide + Ac-Leu-Gly-Lys-7-amido-4-methylcoumarin + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + AFNQG(N6-malonyl)KIFK
nicotinamide + AFNQGKIFK + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + AYVDDTPAEQM(N6-malonyl)KAER
nicotinamide + AYVDDTPAEQMKAER + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-acetyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-adipoyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-adipoyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-glutaryl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-glutaryl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-malonyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-oxalyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-oxalyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-pimeloyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-pimeloyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-suberoyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-suberoyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-succinyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-RGVL(N6-succinyl)KEYGV-amide
nicotinamide + benzoyl-RGVLKEYGV-amide + 2'-O-acetyl-ADP-ribose
carbamoyl phosphate synthetase 1 Lys527 peptide
-
-
?
NAD+ + benzyl-(N6-succinyl)Lys-7-amido-4-methylcoumarin
nicotinamide + benzyl-Lys-7-amido-4-methylcoumarin + 2'-O-succinyl-ADP-ribose
fluorogenic substrate
-
-
?
NAD+ + DSYVGDEAQSDSYVGDEAQS(N6-malonyl)KR
nicotinamide + DSYVGDEAQSDSYVGDEAQSKR + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + ETGVDLT(N6-succinyl)KDNMALQR
nicotinamide + ETGVDLTKDNMALQR + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + IEEELGS(N6-malonyl)KAK
nicotinamide + IEEELGSKAK + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + KGLGKGGA(N6-propionyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-propionyl-ADP-ribose
NAD+ + KGLGKGGA(N6-succinyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-succinyl-ADP-ribose
NAD+ + KQTAR(N6-malonyl)KSTGGWW
nicotinamide + KQTARKSTGGWW + 2'-O-malonyl-ADP-ribose
histone H3K9 malonyl peptide
-
-
?
NAD+ + KQTAR(N6-succinyl)KSTGGKA
nicotinamide + KQTARKSTGGKA + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + KQTAR(N6-succinyl)KSTGGWW
nicotinamide + KQTARKSTGGWW + 2'-O-succinyl-ADP-ribose
histone H3K9 succinyl peptide
-
-
?
NAD+ + KTRSG(N6-malonyl)KVMRRWW
nicotinamide + KTRSGKVMRRWW + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + KTRSG(N6-succinyl)KVMRRWW
nicotinamide + KTRSGKVMRRWW + 2'-O-succinyl-ADP-ribose
ACS2 Lys628 peptide
-
-
?
NAD+ + N2-benzyloxycarbonyl-N6-succinyl-L-lysine-7-amido-4-methylcoumarin
nicotinamide + N2-benzyloxycarbonyl-L-lysine-7-amido-4-methylcoumarin + 2'-O-succinyl-ADP-ribose
i.e. 3-[(5-[[(benzyloxy)carbonyl]amino]-5-[(4-methyl-2-oxo-2H-chromen-7-yl)carbamoyl]pentyl)carbamoyl]-propanoic acid
-
-
?
NAD+ + QTAR(N6-acetyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-acetyl-ADP-ribose
acetylated histone H3 peptide, less than 10% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-decanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-decanoyl-ADP-ribose
decanoylated histone H3 peptide, about 35% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-dodecanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-dodecanoyl-ADP-ribose
dodecanoylated histone H3 peptide, about 35% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-hexanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-hexanoyl-ADP-ribose
hexanoylated histone H3 peptide, less than 10% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-myristoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-myristoyl-ADP-ribose
myristoylated histone H3 peptide, about 15% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-octanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-octanoyl-ADP-ribose
octanoylated histone H3 peptide, about 30% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-propionyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-propionyl-ADP-ribose
propionylated histone H3 peptide, less than 10% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-succinyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-succinyl-ADP-ribose
succinylated histone H3 peptide
-
-
?
NAD+ + SGASE(N6-malonyl)KDIVHSGWW
nicotinamide + SGASEKDIVHSGWW + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + SGASE(N6-succinyl)KDIVHSGWW
nicotinamide + SGASEKDIVHSGWW + 2'-O-succinyl-ADP-ribose
glutamate dehydrogenase Lys503 peptide
-
-
?
NAD+ + SKEYFS(N6-succinyl)KQK
nicotinamide + SKEYFSKQK + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + SQG(N6-succinyl)KVLQATVV
nicotinamide + SQGKVLQATVV + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + TAIG(N6-malonyl)KAGYTDK
nicotinamide + TAIGKAGYTDK + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + TRSG(N6-acetyl)KVMR
nicotinamide + TRSGKVMR + 2'-O-acetyl-ADP-ribose
peptide based on an acetyl-CoA synthetase 2 acetylation site
-
-
?
NAD+ + VLLPEYGGT(N6-succinyl)KVVLDDK
nicotinamide + VLLPEYGGTKVVLDDK + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609
nicotinamide + [acetyl-coenzyme A synthetase]-L-lysine609 + 2'-O-acetyl-ADP-ribose
NAD+ + [ATP synthase]-N6-succinyl-L-lysine
nicotinamide + [ATP synthase]-L-lysine + 2'-O-succinyl-ADP-ribose
NAD+ + [bovine serum albumin]-N6-acetyl-L-lysine
nicotinamide + [bovine serum albumin]-L-lysine + 2'-O-acetyl-ADP-ribose
crystallographic evidence is provided that 2'-O-acetyl ADP-ribose is a final product in the Sir2 reaction. A revised mechanism for catalysis based on the structural and functional characterization of Sir2 mutants is proposed. In this mechanism, the activation of the 2'-OH of nicotinamide ribose by His-116 is essential for the hydrolysis of the acetyl groups from N-acetyl lysine. The conserved Ser-24 and Asp-101 participate in the stabilization of local structure for NAD binding rather than direct involvement in catalysis
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP ribose
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [carbamoyl phosphate synthase 1]-N6-succinyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-succinyl-ADP ribose
deletion of Sirt5 in mice increases the level of succinylation on carbamoyl phosphate synthase 1
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1 derived glutarylated peptide]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1 derived glutarylated peptide]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP ribose
NAD+ + [carbamoyl phosphate synthetase 1]-N6-glutaryl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-glutaryl-ADP-ribose
-
-
-
?
NAD+ + [chicken histone]-N6-acetyl-L-lysine
nicotinamide + [chicken histone]-L-lysine + 2'-O-acetyl-ADP-ribose
chemically acetylated chicken histone. Less activity toward chemically acetylated bovine serum albumin and monoacetylated histone H4 (K16 and K8). No activity is observed with monoacetylated histone K5 and K12 histone H4 peptides
-
-
?
NAD+ + [Cu/Zn superoxide dismutase]-N6-succinyl-L-lysine123
nicotinamide + [Cu/Zn superoxide dismutase]-L-lysine123 + 2'-O-succinyl-ADP-ribose
NAD+ + [cytochrome c]-N6-acetyl-L-lysine
nicotinamide + [cytochrome c]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [forkhead box O3]-N6-acetyl-L-lysine
nicotinamide + [forkhead box O3]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme deacetylates FOXO3 at K271 and K290
-
-
?
NAD+ + [glucose 6-phosphate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [glucose 6-phosphate dehydrogenase]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [glucose-6-phosphate dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [glucose-6-phosphate dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [glutaminase]-N6-succinyl-L-lysine
nicotinamide + [glutaminase]-L-lysine + 2'-O-succinyl-ADP-ribose
NAD+ + [glyceraldehyde-3-phosphate dehydrogenase]-N6-malonyl-L-lysine
nicotinamide + [glyceraldehyde-3-phosphate dehydrogenase]-L-lysine + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + [histone H2A]-N6-succinyl-L-lysine95
nicotinamide + [histone H2A]-L-lysine95 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [histone H2A]-N6-succinyl-L-lysine9_(4-15)-A10G peptide
nicotinamide + [histone H2A]-L-lysine9_(4-15)-A10G peptide + 2'-O-succinyl-ADP-ribose
partial desuccinylation, mutant peptide substrate
-
-
?
NAD+ + [histone H2B]-N6-succinyl-L-lysine116
nicotinamide + [histone H2B]-L-lysine116 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [histone H2B]-N6-succinyl-L-lysine120
nicotinamide + [histone H2B]-L-lysine120 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [histone H2B]-N6-succinyl-L-lysine34
nicotinamide + [histone H2B]-L-lysine34 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [histone H2B]-N6-succinyl-L-lysine9
nicotinamide + [histone H2B]-L-lysine9 + 2'-O-succinyl-ADP-ribose
NAD+ + [histone H3 K9 peptide]-N6-acetyl-L-lysine
nicotinamide + [histone H3 K9 peptide]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [histone H3 K9 peptide]-N6-succinyl-L-lysine
nicotinamide + [histone H3 K9 peptide]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [histone H3]-N6-succinyl-L-lysine122
nicotinamide + [histone H3]-L-lysine122 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [histone H3]-N6-succinyl-L-lysine14
nicotinamide + [histone H3]-L-lysine14 + 2'-O-succinyl-ADP-ribose
partial desuccinylation, low activity
-
-
?
NAD+ + [histone H3]-N6-succinyl-L-lysine14_(9-20)-A15G peptide
nicotinamide + [histone H3]-L-lysine14_(9-20)-A15G peptide + 2'-O-succinyl-ADP-ribose
partial desuccinylation, mutant peptide substrate
-
-
?
NAD+ + [histone H3]-N6-succinyl-L-lysine56
nicotinamide + [histone H3]-L-lysine56 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [histone H3]-N6-succinyl-L-lysine79
nicotinamide + [histone H3]-L-lysine79 + 2'-O-succinyl-ADP-ribose
partial desuccinylation
-
-
?
NAD+ + [histone H3]-N6-succinyl-L-lysine9
nicotinamide + [histone H3]-L-lysine9 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [histone H4]-N6-acetyl-L-lysine16
nicotinamide + [histone H4]-L-lysine16 + 2'-O-acetyl-ADP-ribose
deacetylation, cf. EC 2.3.1.286
-
-
?
NAD+ + [histone H4]-N6-succinyl-L-lysine12
nicotinamide + [histone H4]-L-lysine12 + 2'-O-succinyl-ADP-ribose
partial desuccinylation
-
-
?
NAD+ + [histone H4]-N6-succinyl-L-lysine31
nicotinamide + [histone H4]-L-lysine31 + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [histone H4]-N6-succinyl-L-lysine31_(26-37)-P32A peptide
nicotinamide + [histone H4]-L-lysine31_(26-37)-P32A peptide + 2'-O-succinyl-ADP-ribose
partial desuccinylation, mutant peptide substrate
-
-
?
NAD+ + [histone H4]-N6-succinyl-L-lysine77
nicotinamide + [histone H4]-L-lysine77 + 2'-O-succinyl-ADP-ribose
almost complete desuccinylation
-
-
?
NAD+ + [histone H4]-N6-succinyl-L-lysine91
nicotinamide + [histone H4]-L-lysine91 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [IDH2]-N6-succinyl-L-lysine
nicotinamide + [IDH2]-L-lysine + 2'-O-succinyl-ADP-ribose
i.e. isocitrate dehydrogenase [NADP+]
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [peptide derived from carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [peptide derived from carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
NAD+ + [PrpE protein]-N6-acetyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-acetyl-ADP ribose
-
-
-
-
?
NAD+ + [PrpE protein]-N6-propionyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-propionyl-ADP-ribose
NAD+ + [pyruvate dehydrogenase complex]-N6-succinyl-L-lysine
nicotinamide + [pyruvate dehydrogenase complex]-L-lysine + O-succinyl-ADP-ribose
NAD+ + [pyruvate kinase M2]-N6-succinyl-L-lysine311
nicotinamide + [pyruvate kinase M2]-L-lysine311 + 2'-O-succinyl-ADP-ribose
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [succinate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [succinate dehydrogenase]-L-lysine + O-succinyl-ADP-ribose
NAD+ + [urate oxidase]-N6-acetyl-L-lysine
nicotinamide + [urate oxidase]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + FKRGVL(N6-acetyl)KEYGVKV
nicotinamide + FKRGVLKEYGVKV + 2'-O-acetyl-ADP-ribose
acetylated peptide derived from carbamoylphosphate synthetase 1 (CPS1)
-
-
?
NAD+ + FKRGVL(N6-acetyl)KEYGVKV
nicotinamide + FKRGVLKEYGVKV + 2'-O-acetyl-ADP-ribose
carbamoyl phosphate synthetase 1 Lys527 peptide
-
-
?
NAD+ + KGLGKGGA(N6-acetyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-acetyl-ADP-ribose
the rate of desuccinylation is about 5fold faster than the rate of deacetylation
-
-
?
NAD+ + KGLGKGGA(N6-acetyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-acetyl-ADP-ribose
-
the rate of desuccinylation is 2.3fold faster than the rate of deacetylation
-
-
?
NAD+ + KGLGKGGA(N6-butyryl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-butyryl-ADP-ribose
the rate of desuccinylation is about 10fold faster than the rate of debutyrylation
-
-
?
NAD+ + KGLGKGGA(N6-butyryl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-butyryl-ADP-ribose
-
the rate of desuccinylation is 5.8fold faster than the rate of deburyrylation
-
-
?
NAD+ + KGLGKGGA(N6-propionyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-propionyl-ADP-ribose
the rate of desuccinylation is about 5fold faster than the rate of depropionylation
-
-
?
NAD+ + KGLGKGGA(N6-propionyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-propionyl-ADP-ribose
-
the rate of desuccinylation is 3.8fold faster than the rate of depropionylation
-
-
?
NAD+ + KGLGKGGA(N6-succinyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-succinyl-ADP-ribose
the rate of desuccinylation is about 5fold faster than the rate of deacetylation
-
-
?
NAD+ + KGLGKGGA(N6-succinyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-succinyl-ADP-ribose
-
the rate of desuccinylation is 2.3fold faster than the rate of deacetylation
-
-
?
NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609
nicotinamide + [acetyl-coenzyme A synthetase]-L-lysine609 + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609
nicotinamide + [acetyl-coenzyme A synthetase]-L-lysine609 + 2'-O-acetyl-ADP-ribose
-
deacetylation by CobB activates the acetyl-coenzyme A synthetase
-
-
?
NAD+ + [ATP synthase]-N6-succinyl-L-lysine
nicotinamide + [ATP synthase]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [ATP synthase]-N6-succinyl-L-lysine
nicotinamide + [ATP synthase]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP ribose
-
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP ribose
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle. Deacetylation of CPS1 by SIRT5 results in activation of CPS1 enzymatic activity
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP ribose
-
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP ribose
SIRT5 plays a pivotal role in ammonia detoxification and disposal by activating carbamoyl phosphate synthetase 1 (CPS1) an enzyme, catalyzing the initial step of the urea cycle for ammonia detoxification and disposal. SIRT5 deacetylates CPS1 and up-regulates its activity. During fasting, NAD+ in liver mitochondria increases, thereby triggering SIRT5 deacetylation of CPS1 and adaptation to the increase in amino acid catabolism. Indeed, SIRT5 KO mice fail to up-regulate CPS1 activity and show elevated blood ammonia during fasting
-
-
?
NAD+ + [Cu/Zn superoxide dismutase]-N6-succinyl-L-lysine123
nicotinamide + [Cu/Zn superoxide dismutase]-L-lysine123 + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [Cu/Zn superoxide dismutase]-N6-succinyl-L-lysine123
nicotinamide + [Cu/Zn superoxide dismutase]-L-lysine123 + 2'-O-succinyl-ADP-ribose
SIRT5 binds to, desuccinylates and activates the key antioxidant enzyme Cu/Zn superoxide dismutase (SOD1). SOD1-mediated reduction of reactive oxygen species (ROS) is increased when SIRT5 is co-expressed. Posttranslational regulation of SOD1 by means of succinylation and SIRT5-dependent desuccinylation is important for the growth of lung tumor cells
-
-
?
NAD+ + [glutaminase]-N6-succinyl-L-lysine
nicotinamide + [glutaminase]-L-lysine + 2'-O-succinyl-ADP-ribose
SIRT5 desuccinylates glutaminase residue K164 to block ubiquitination of K158
-
-
?
NAD+ + [glutaminase]-N6-succinyl-L-lysine
nicotinamide + [glutaminase]-L-lysine + 2'-O-succinyl-ADP-ribose
succinylation of glutaminase residue K164, no activity with K164R-GLS variant
-
-
?
NAD+ + [histone H2B]-N6-succinyl-L-lysine9
nicotinamide + [histone H2B]-L-lysine9 + 2'-O-succinyl-ADP-ribose
partial desuccinylation
-
-
?
NAD+ + [histone H2B]-N6-succinyl-L-lysine9
nicotinamide + [histone H2B]-L-lysine9 + 2'-O-succinyl-ADP-ribose
partial desuccinylation
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
the enzyme regulates protein function in diverse and often essential cellular processes, most notably translation
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
the enzyme can deacetylate acetyllysine independently whether the acetyl donor is acetyl-Coenzyme A or acetyl phosphate. Linear sequences alone are inadequate to predict CobB substrates and that structural analyses are necessary. CobB substrate acetyllyines appear to be located near the surface of the protein on a
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
weak deacetylase activity
-
-
?
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
protein lysine succinylation may represent a posttranslational modification that can be reversed by Sirt5 in vivo. Lysine succinylation occurs on several mammalian proteins
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
strong succinylase activity
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [PrpE protein]-N6-propionyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-propionyl-ADP-ribose
-
-
-
-
?
NAD+ + [PrpE protein]-N6-propionyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-propionyl-ADP-ribose
-
N-Lysine propionylation controls the activity of propionyl-CoA synthetase
-
-
?
NAD+ + [pyruvate dehydrogenase complex]-N6-succinyl-L-lysine
nicotinamide + [pyruvate dehydrogenase complex]-L-lysine + O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [pyruvate dehydrogenase complex]-N6-succinyl-L-lysine
nicotinamide + [pyruvate dehydrogenase complex]-L-lysine + O-succinyl-ADP-ribose
SIRT5 represses biochemical activity of, and cellular respiration through, the protein complex
-
-
?
NAD+ + [pyruvate kinase M2]-N6-succinyl-L-lysine311
nicotinamide + [pyruvate kinase M2]-L-lysine311 + 2'-O-succinyl-ADP-ribose
SIRT5 desuccinylates and activates PKM2
-
-
?
NAD+ + [pyruvate kinase M2]-N6-succinyl-L-lysine311
nicotinamide + [pyruvate kinase M2]-L-lysine311 + 2'-O-succinyl-ADP-ribose
SIRT5 also desuccinylates recombinant Flag-tagged PKM2 substrate, but does not but affect its malonylation and glutarylation. The K311E mutation and K311E/K498E double mutation of PKM2 both increase the succinylation level of PKM2 by about 25%, while mutations K62R/E, K135R/E, and K498R/E have no significant effect
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
acetylation of the response regulator RcsB controls transcription from the small RNA promoter rprA
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
reversible Nepsilon-Lys acetylation of transcription factors is a mode of regulation of gene expression used by all cells
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
Escherichia coli W3110 / ATCC 27325
-
-
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
Escherichia coli W3110 / ATCC 27325
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
-
-
?
NAD+ + [succinate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [succinate dehydrogenase]-L-lysine + O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [succinate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [succinate dehydrogenase]-L-lysine + O-succinyl-ADP-ribose
SIRT5 represses biochemical activity of, and cellular respiration through, the protein complex
-
-
?
NAD+ + [urate oxidase]-N6-acetyl-L-lysine
nicotinamide + [urate oxidase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [urate oxidase]-N6-acetyl-L-lysine
nicotinamide + [urate oxidase]-L-lysine + 2'-O-acetyl-ADP-ribose
SIRT5 activates urate oxidase through deacetylation in mouse liver mitochondria
-
-
?
additional information
?
-
-
it is proposed that YfiQ and CobB catalyze the reversible acetylation of a protein that mediates carbon-induced cpxP transcription
-
-
?
additional information
?
-
-
global identification of CobB substrates using an Escherichia coli proteome microarray
-
-
?
additional information
?
-
-
the enzyme shows dual enzymatic activities to catalyze the removal of two structurally different lysine acyl groups, acetyl and succinyl, from the modified lysine residues
-
-
?
additional information
?
-
-
global identification of CobB substrates using an Escherichia coli proteome microarray
-
-
?
additional information
?
-
catalytic efficiency (kcat/Km) of Sirt5 with the histone H3K9 acetyl peptide is about 500fold lower than that of Sirt1. Sirtuin 5 has only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr102 and Arg105) that bind to malonylated and succinylated substrates and define the specificity
-
-
?
additional information
?
-
no activity with Ac-Leu-Gly-(N6-acetyl)Lys-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
no activity with Ac-Leu-Gly-(N6-acetyl)Lys-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
Sirt5 does not deacetylate glutamate dehydrogenase or isocitrate dehydrogenase 2
-
-
?
additional information
?
-
-
Sirt5 does not deacetylate glutamate dehydrogenase or isocitrate dehydrogenase 2
-
-
?
additional information
?
-
Sirt5 catalyzes the desuccinylation of histone peptides, molecular mechanism, overview. Human Sirt5 is a ubiquitous desuccinylase that catalyzes the desuccinylation of diverse histone succinyl sites with sequence selectivity. Among the 13 identified sites, H2BK116su is the most favorable Sirt5 substrate, with H4K12su showing the lowest catalytic efficiency and no activity observed in the presence of H4K31su
-
-
-
additional information
?
-
-
Sirt5 catalyzes the desuccinylation of histone peptides, molecular mechanism, overview. Human Sirt5 is a ubiquitous desuccinylase that catalyzes the desuccinylation of diverse histone succinyl sites with sequence selectivity. Among the 13 identified sites, H2BK116su is the most favorable Sirt5 substrate, with H4K12su showing the lowest catalytic efficiency and no activity observed in the presence of H4K31su
-
-
-
additional information
?
-
SIRT5 catalyzes the removal of negatively charged lysine acyl modifications: succinyl, malonyl, and glutaryl groups. SIRT5 is selective only for 3-5 carbon chains acidic acyl modifications, and displays no detectable activity against either an acetyl modification, a neutral 2 carbon group, or an adipoyl, a 6-carbon acidic modification
-
-
-
additional information
?
-
SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II. Mass spectrometry identifies 14 SIRT5 target sites on the SDHA subunit of Complex II and another eight on SDHB. Molecular modeling reveals that six of the eight SIRT5 target sites on SDHB orient toward the predicted membrane interface where SDHB interacts with SDHC/SDHD
-
-
-
additional information
?
-
-
SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II. Mass spectrometry identifies 14 SIRT5 target sites on the SDHA subunit of Complex II and another eight on SDHB. Molecular modeling reveals that six of the eight SIRT5 target sites on SDHB orient toward the predicted membrane interface where SDHB interacts with SDHC/SDHD
-
-
-
additional information
?
-
essential role for the conserved main chain hydrogen bonds formed by the succinyl lysine (0), +1, and +3 sites for substrate-enzyme recognition. A proline residue at the +1 site of the histone succinylation substrate is unfavorable for Sirt5 interaction. Molecular mechanism underlying the sequence-selective desuccinylase activity of Sirt5, overview. No activity with H4K31su, and mutant substrates H3K9(4-15)-S10Psu and H3K56(51-62)-S57Psu. Usage of peptides of histone substrates
-
-
-
additional information
?
-
-
essential role for the conserved main chain hydrogen bonds formed by the succinyl lysine (0), +1, and +3 sites for substrate-enzyme recognition. A proline residue at the +1 site of the histone succinylation substrate is unfavorable for Sirt5 interaction. Molecular mechanism underlying the sequence-selective desuccinylase activity of Sirt5, overview. No activity with H4K31su, and mutant substrates H3K9(4-15)-S10Psu and H3K56(51-62)-S57Psu. Usage of peptides of histone substrates
-
-
-
additional information
?
-
synthsis of substrate peptide (2-Abz)-GVLK (succ)A [Y (3-NO2)]GV-NH2
-
-
-
additional information
?
-
-
synthsis of substrate peptide (2-Abz)-GVLK (succ)A [Y (3-NO2)]GV-NH2
-
-
-
additional information
?
-
Sirt5 shows negligible activity toward lysine deacetylation
-
-
?
additional information
?
-
SIRT5 catalyzes the removal of negatively charged lysine acyl modifications: succinyl, malonyl, and glutaryl groups. SIRT5 is selective only for 3-5 carbon chains acidic acyl modifications, and displays no detectable activity against either an acetyl modification, a neutral 2 carbon group, or an adipoyl, a 6-carbon acidic modification
-
-
-
additional information
?
-
SIRT5 modifies lysine succinylation, malonylation, and glutarylation
-
-
-
additional information
?
-
three-dimensional modeling of Complex II suggests that several SIRT5-targeted lysine residues lie at the protein-lipid interface of succinate dehydrogenase subunit B. Succinylation at these sites may disrupt Complex II subunit-subunit interactions and electron transfer. SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II
-
-
-
additional information
?
-
-
three-dimensional modeling of Complex II suggests that several SIRT5-targeted lysine residues lie at the protein-lipid interface of succinate dehydrogenase subunit B. Succinylation at these sites may disrupt Complex II subunit-subunit interactions and electron transfer. SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II
-
-
-
additional information
?
-
protein malonylation and succinylation lysine sites are identified by immunoprecipitation coupled lipid chromatography-tandem mass spectrometry (LC-MS/MS) methods
-
-
-
additional information
?
-
-
protein malonylation and succinylation lysine sites are identified by immunoprecipitation coupled lipid chromatography-tandem mass spectrometry (LC-MS/MS) methods
-
-
-
additional information
?
-
protein malonylation and succinylation lysine sites are identified by immunoprecipitation coupled lipid chromatography-tandem mass spectrometry (LC-MS/MS) methods
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609
nicotinamide + [acetyl-coenzyme A synthetase]-L-lysine609 + 2'-O-acetyl-ADP-ribose
-
deacetylation by CobB activates the acetyl-coenzyme A synthetase
-
-
?
NAD+ + [ATP synthase]-N6-succinyl-L-lysine
nicotinamide + [ATP synthase]-L-lysine + 2'-O-succinyl-ADP-ribose
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP ribose
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle. Deacetylation of CPS1 by SIRT5 results in activation of CPS1 enzymatic activity
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-succinyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-succinyl-ADP ribose
deletion of Sirt5 in mice increases the level of succinylation on carbamoyl phosphate synthase 1
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP ribose
SIRT5 plays a pivotal role in ammonia detoxification and disposal by activating carbamoyl phosphate synthetase 1 (CPS1) an enzyme, catalyzing the initial step of the urea cycle for ammonia detoxification and disposal. SIRT5 deacetylates CPS1 and up-regulates its activity. During fasting, NAD+ in liver mitochondria increases, thereby triggering SIRT5 deacetylation of CPS1 and adaptation to the increase in amino acid catabolism. Indeed, SIRT5 KO mice fail to up-regulate CPS1 activity and show elevated blood ammonia during fasting
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-glutaryl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-glutaryl-ADP-ribose
-
-
-
?
NAD+ + [Cu/Zn superoxide dismutase]-N6-succinyl-L-lysine123
nicotinamide + [Cu/Zn superoxide dismutase]-L-lysine123 + 2'-O-succinyl-ADP-ribose
SIRT5 binds to, desuccinylates and activates the key antioxidant enzyme Cu/Zn superoxide dismutase (SOD1). SOD1-mediated reduction of reactive oxygen species (ROS) is increased when SIRT5 is co-expressed. Posttranslational regulation of SOD1 by means of succinylation and SIRT5-dependent desuccinylation is important for the growth of lung tumor cells
-
-
?
NAD+ + [forkhead box O3]-N6-acetyl-L-lysine
nicotinamide + [forkhead box O3]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme deacetylates FOXO3 at K271 and K290
-
-
?
NAD+ + [glucose 6-phosphate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [glucose 6-phosphate dehydrogenase]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [glucose-6-phosphate dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [glucose-6-phosphate dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [glutaminase]-N6-succinyl-L-lysine
nicotinamide + [glutaminase]-L-lysine + 2'-O-succinyl-ADP-ribose
SIRT5 desuccinylates glutaminase residue K164 to block ubiquitination of K158
-
-
?
NAD+ + [histone H2B]-N6-succinyl-L-lysine9
nicotinamide + [histone H2B]-L-lysine9 + 2'-O-succinyl-ADP-ribose
partial desuccinylation
-
-
?
NAD+ + [histone H4]-N6-acetyl-L-lysine16
nicotinamide + [histone H4]-L-lysine16 + 2'-O-acetyl-ADP-ribose
deacetylation, cf. EC 2.3.1.286
-
-
?
NAD+ + [IDH2]-N6-succinyl-L-lysine
nicotinamide + [IDH2]-L-lysine + 2'-O-succinyl-ADP-ribose
i.e. isocitrate dehydrogenase [NADP+]
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
NAD+ + [PrpE protein]-N6-propionyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-propionyl-ADP-ribose
-
N-Lysine propionylation controls the activity of propionyl-CoA synthetase
-
-
?
NAD+ + [pyruvate dehydrogenase complex]-N6-succinyl-L-lysine
nicotinamide + [pyruvate dehydrogenase complex]-L-lysine + O-succinyl-ADP-ribose
SIRT5 represses biochemical activity of, and cellular respiration through, the protein complex
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?
NAD+ + [pyruvate kinase M2]-N6-succinyl-L-lysine311
nicotinamide + [pyruvate kinase M2]-L-lysine311 + 2'-O-succinyl-ADP-ribose
SIRT5 desuccinylates and activates PKM2
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?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [succinate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [succinate dehydrogenase]-L-lysine + O-succinyl-ADP-ribose
SIRT5 represses biochemical activity of, and cellular respiration through, the protein complex
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?
NAD+ + [urate oxidase]-N6-acetyl-L-lysine
nicotinamide + [urate oxidase]-L-lysine + 2'-O-acetyl-ADP-ribose
SIRT5 activates urate oxidase through deacetylation in mouse liver mitochondria
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?
NAD+ + [ATP synthase]-N6-succinyl-L-lysine
nicotinamide + [ATP synthase]-L-lysine + 2'-O-succinyl-ADP-ribose
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?
NAD+ + [ATP synthase]-N6-succinyl-L-lysine
nicotinamide + [ATP synthase]-L-lysine + 2'-O-succinyl-ADP-ribose
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?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
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?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
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?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
the enzyme regulates protein function in diverse and often essential cellular processes, most notably translation
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?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
weak deacetylase activity
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?
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
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?
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
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?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
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?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
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?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
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?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
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?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
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?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
protein lysine succinylation may represent a posttranslational modification that can be reversed by Sirt5 in vivo. Lysine succinylation occurs on several mammalian proteins
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?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
strong succinylase activity
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?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
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?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
acetylation of the response regulator RcsB controls transcription from the small RNA promoter rprA
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?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
reversible Nepsilon-Lys acetylation of transcription factors is a mode of regulation of gene expression used by all cells
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?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
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the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
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?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
Escherichia coli W3110 / ATCC 27325
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the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
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?
additional information
?
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it is proposed that YfiQ and CobB catalyze the reversible acetylation of a protein that mediates carbon-induced cpxP transcription
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?
additional information
?
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Sirt5 catalyzes the desuccinylation of histone peptides, molecular mechanism, overview. Human Sirt5 is a ubiquitous desuccinylase that catalyzes the desuccinylation of diverse histone succinyl sites with sequence selectivity. Among the 13 identified sites, H2BK116su is the most favorable Sirt5 substrate, with H4K12su showing the lowest catalytic efficiency and no activity observed in the presence of H4K31su
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additional information
?
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Sirt5 catalyzes the desuccinylation of histone peptides, molecular mechanism, overview. Human Sirt5 is a ubiquitous desuccinylase that catalyzes the desuccinylation of diverse histone succinyl sites with sequence selectivity. Among the 13 identified sites, H2BK116su is the most favorable Sirt5 substrate, with H4K12su showing the lowest catalytic efficiency and no activity observed in the presence of H4K31su
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additional information
?
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SIRT5 catalyzes the removal of negatively charged lysine acyl modifications: succinyl, malonyl, and glutaryl groups. SIRT5 is selective only for 3-5 carbon chains acidic acyl modifications, and displays no detectable activity against either an acetyl modification, a neutral 2 carbon group, or an adipoyl, a 6-carbon acidic modification
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additional information
?
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SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II. Mass spectrometry identifies 14 SIRT5 target sites on the SDHA subunit of Complex II and another eight on SDHB. Molecular modeling reveals that six of the eight SIRT5 target sites on SDHB orient toward the predicted membrane interface where SDHB interacts with SDHC/SDHD
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additional information
?
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SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II. Mass spectrometry identifies 14 SIRT5 target sites on the SDHA subunit of Complex II and another eight on SDHB. Molecular modeling reveals that six of the eight SIRT5 target sites on SDHB orient toward the predicted membrane interface where SDHB interacts with SDHC/SDHD
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additional information
?
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SIRT5 catalyzes the removal of negatively charged lysine acyl modifications: succinyl, malonyl, and glutaryl groups. SIRT5 is selective only for 3-5 carbon chains acidic acyl modifications, and displays no detectable activity against either an acetyl modification, a neutral 2 carbon group, or an adipoyl, a 6-carbon acidic modification
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additional information
?
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SIRT5 modifies lysine succinylation, malonylation, and glutarylation
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additional information
?
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three-dimensional modeling of Complex II suggests that several SIRT5-targeted lysine residues lie at the protein-lipid interface of succinate dehydrogenase subunit B. Succinylation at these sites may disrupt Complex II subunit-subunit interactions and electron transfer. SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II
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additional information
?
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three-dimensional modeling of Complex II suggests that several SIRT5-targeted lysine residues lie at the protein-lipid interface of succinate dehydrogenase subunit B. Succinylation at these sites may disrupt Complex II subunit-subunit interactions and electron transfer. SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
the zinc-binding domain of the sirtuin proteins may play a similar role in substrate-specific recognition
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-2-[(naphthalen-2-yl)sulfanyl]-4-oxo-4-[(3-phenylpropyl)amino]butanoic acid
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(2S)-4-[3-(methylcarbamoyl)anilino]-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
-
(2S)-4-[[(5S)-5-acetamido-6-amino-6-oxohexyl]amino]-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
-
(3E)-3-[(3,5-dibromo-4-hydroxyphenyl)methylidene]-5-iodo-1,3-dihydro-2H-indol-2-one
-
(5E)-1-ethyl-5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
(5E)-5-(1H-indol-3-ylmethylidene)-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
(5E)-5-[4-(benzyloxy)benzylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
(5E)-5-[4-(benzyloxy)benzylidene]-1-ethyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
(5E)-5-[4-(benzyloxy)benzylidene]-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
(5E)-5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-1-(prop-2-en-1-yl)-2-sulfanylidene-1,3-diazinane-4,6-dione
-
(5E)-5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
1-(2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)-3-phenylurea
10% inhibition at 0.1 mM
2-cyano-3-[5-(4-cyanophenyl)furan-2-yl]-N-(3,4-dimethylphenyl)propanamide
-
2-cyano-N-(3,4-dimethylphenyl)-3-[5-(4-nitrophenyl)furan-2-yl]propanamide
-
3',5'-dimethyl-1'-phenyl-1H,1'H-[3,4'-bipyrazole]-5-carboxylic acid
21.54% inhibition at 0.1 mM
3-(((2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)amino)methyl)benzoic acid
32% inhibition at 0.1 mM
3-((2-(9H-pyrido[3,4-b]indol-9-yl)acetamido)methyl)benzoic acid
21% inhibition at 0.1 mM
3-((2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)carbamoyl)benzoicacid
15% inhibition at 0.1 mM
3-(3,5-dibromo-4-hydroxybenzyliden)-5-iodo-1,3-dihydroindol-2-one
i.e. GW5074, potent inhibitor for desuccinylation activity of Sirt5. 0.1 mM inhibitor reduces Sirt5 desuccinylation activity (substrate: SKEYFS-(succinylLys)-QK) to about 15%. Weaker effects in Sirt5 deacetylation assays. Deacetylation activity is reduced to about 30% in presence of 0.1 mM inhibitor
3-(3-(2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)ureido)benzoic acid
36% inhibition at 0.1 mM
3-chloro-5-(3,4-dimethoxyphenyl)-7-(trifluoromethyl)pyrazolo[1,5-a]pyrimidine-2-carboxylic acid
30.85% inhibition at 0.1 mM
3-hydroxy-5-(morpholine-4-sulfonyl)naphthalene-2-carboxylic acid
9.2% inhibition at 0.1 mM
3-hydroxy-5-[(prop-2-en-1-yl)sulfamoyl]naphthalene-2-carboxylic acid
17.43% inhibition at 0.1 mM
3-[5-[2-cyano-3-(3,4-dimethylanilino)-3-oxopropyl]furan-2-yl]benzoic acid
-
4-(((2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)amino)methyl)benzoic acid
22% inhibition at 0.1 mM
4-((2-(9H-pyrido[3,4-b]indol-9-yl)acetamido)methyl)benzoic acid
25% inhibition at 0.1 mM
4-((2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)carbamoyl)benzoic acid
25% inhibition at 0.1 mM
4-(3,4-dimethyl-6-oxopyrano[2,3-c]pyrazol-1(6H)-yl)benzoic acid
18.70% inhibition at 0.1 mM
4-(3-(2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)ureido)benzoic acid
52% inhibition at 0.1 mM
4-(5-[(Z)-[1-(3-chloro-4-methylphenyl)-3-methyl-5-oxo-1,5-dihydro-4H-pyrazol-4-ylidene]methyl]furan-2-yl)benzoic acid
94.3% inhibition at 0.1 mM
4-(5-[2-cyano-3-[(2,3-dihydro-1,4-benzodioxin-6-yl)amino]-3-oxopropyl]furan-2-yl)benzoic acid
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4-(5-[2-cyano-3-[3-(methylcarbamoyl)anilino]-3-oxopropyl]furan-2-yl)benzoic acid
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4-(5-[2-cyano-3-[4-cyano-3-(trifluoromethyl)anilino]-3-oxopropyl]furan-2-yl)benzoic acid
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4-(5-[3-[(2H-1,3-benzodioxol-5-yl)amino]-2-cyano-3-oxopropyl]furan-2-yl)benzoic acid
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4-(5-[3-[4-chloro-3-(trifluoromethyl)anilino]-2-cyano-3-oxopropyl]furan-2-yl)benzoic acid
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4-(6-tert-butyl-2H-1,3-benzoxazin-3(4H)-yl)benzoic acid
24.54% inhibition at 0.1 mM
4-([(Z)-[2-(2-bromophenyl)-5-oxo-1,3-oxazol-4(5H)-ylidene]methyl]amino)benzoic acid
34.24% inhibition at 0.1 mM
4-[(4Z)-3-methyl-5-oxo-4-[(2E)-3-phenylprop-2-en-1-ylidene]-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
77.26% inhibition at 0.1 mM
4-[(E)-(6-hydroxyquinolin-5-yl)diazenyl]benzoic acid
61.3% inhibition at 0.1 mM
4-[(E)-[(4-bromo-3-chloro-2-hydroxyphenyl)methylidene]amino]benzoic acid
33.66% inhibition at 0.1 mM
4-[5-[(1E)-3-(4-chloro-3-nitroanilino)-2-cyano-3-oxoprop-1-en-1-yl]furan-2-yl]benzoic acid
97.14% inhibition at 0.1 mM
4-[5-[2-cyano-3-(3,4-dimethoxyanilino)-3-oxopropyl]furan-2-yl]benzoic acid
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4-[5-[2-cyano-3-(3,4-dimethylanilino)-3-oxopropyl]furan-2-yl]-3-fluorobenzoic acid
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4-[5-[2-cyano-3-(3,4-dimethylanilino)-3-oxopropyl]furan-2-yl]-3-methylbenzoic acid
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4-[5-[2-cyano-3-(3,4-dimethylanilino)-3-oxopropyl]furan-2-yl]benzoic acid
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4-[5-[2-cyano-3-(3,5-dichloroanilino)-3-oxopropyl]furan-2-yl]benzoic acid
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4-[5-[2-cyano-3-(3,5-dimethylanilino)-3-oxopropyl]furan-2-yl]benzoic acid
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4-[5-[3-(3-acetamidoanilino)-2-cyano-3-oxopropyl]furan-2-yl]benzoic acid
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5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
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5-(4-hydroxy-2,2-dimethyloxan-4-yl)-1,2-oxazole-3-carboxylic acid
17.41% inhibition at 0.1 mM
5-(4-methylphenyl)-7-(trifluoromethyl)pyrazolo[1,5-a]pyrimidine-2-carboxylic acid
11.08% inhibition at 0.1 mM
5-(biphenyl-4-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
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5-[(1-benzyl-1H-indol-3-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
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5-[(5-[[(benzyloxy)carbonyl]amino]-6-[(diphenylmethyl)amino]-6-oxohexyl)amino]-5-sulfanylidenepentanoic acid
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5-[(5-[[(benzyloxy)carbonyl]amino]-6-[[(naphthalen-1-yl)methyl]amino]-6-oxohexyl)amino]-5-sulfanylidenepentanoic acid
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5-[(5-[[(benzyloxy)carbonyl]amino]-6-[[2-(1H-indol-3-yl)ethyl]amino]-6-oxohexyl)amino]-5-sulfanylidenepentanoic acid
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5-[(6-amino-5-[[(benzyloxy)carbonyl]amino]-6-oxohexyl)amino]-5-sulfanylidenepentanoic acid
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5-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
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5-[(6-[(1,3-benzothiazol-5-yl)amino]-5-[[(benzyloxy)carbonyl]amino]-6-oxohexyl)amino]-5-sulfanylidenepentanoic acid
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5-[(6-[(adamantan-1-yl)amino]-5-[[(benzyloxy)carbonyl]amino]-6-oxohexyl)amino]-5-sulfanylidenepentanoic acid
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5-[(E)-(5-hydroxy-3-methyl-1-phenyl-1H-pyrazol-4-yl)diazenyl]-4H-pyrazole-3-carboxylic acid
70.03% inhibition at 0.1 mM
5-[4-(benzyloxy)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
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5-[4-(propan-2-yl)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
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5-[4-[(2-chlorobenzyl)oxy]-3-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
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5-[4-[(4-bromobenzyl)oxy]benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
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5-[[4-(benzyloxy)phenyl]methylidene]-2-sulfanylidene-1,3-diazinane-4,6-dione
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5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
5-[[5-[[(benzyloxy)carbonyl]amino]-6-oxo-6-([(1S)-2-oxo-1-phenyl-2-[(propan-2-yl)amino]ethyl]amino)hexyl]amino]-5-sulfanylidenepentanoic acid
-
6-carboxy-5-methyl-3-[2-(3-methylpiperidin-1-yl)-2-oxoethyl]-4-oxo-4,4a-dihydrothieno[2,3-d]pyrimidin-3-ium
15.43% inhibition at 0.1 mM
7-(diethylamino)-2-oxo-2H-1-benzopyran-3-carboxylic acid
28.91% inhibition at 0.1 mM
ethyl 4-[[2-(9H-pyrido[3,4-b]indol-9-yl)acetamido]methyl]benzoate
12% inhibition at 0.1 mM
L-lysyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-N6-(3-carboxypropanethioyl)-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanine
-
methyl 4-[5-[2-cyano-3-(3,4-dimethylanilino)-3-oxopropyl]furan-2-yl]benzoate
-
N-(4-chlorobenzyl)-2-(9H-pyrido[3,4-b]indol-9-yl)acetamide
18% inhibition at 0.1 mM
N-(pyridin-3-ylmethyl)-2-(9H-pyrido[3,4-b]indol-9-yl)acetamide
24% inhibition at 0.1 mM
N-([4-[(3S,6S,9S)-9-acetamido-27-[[(2S,3R)-1-amino-3-hydroxy-1-oxobutan-2-yl]carbamoyl]-6-(3-carbamimidamidopropyl)-2,5,8,14,21-pentaoxo-1,4,7,13,22-pentaazacycloheptacosan-3-yl]butyl]carbamothioyl)-beta-alanine
-
N-acetyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alaninamide
-
N-acetyl-L-leucyl-N6-[3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alaninamide
-
N-benzyl-2-(9H-pyrido[3,4-b]indol-9-yl)ethan-1-amine
10% inhibition at 0.1 mM
N-benzylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-phenylbutanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-[[2-(pyrazin-2-yl)ethyl]sulfanyl]propanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-[[2-(pyridin-2-yl)ethyl]sulfanyl]propanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-[[2-(pyridin-4-yl)ethyl]sulfanyl]propanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-4-phenylbutanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-(cyclohexylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-([[3-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2,3-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2,6-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2-phenylethyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3,4-dimethylphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3-phenylpropyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(4-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(naphthalen-1-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]butanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(2,4,6-trimethylphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(2,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(2-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(3,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(3-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(4-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(4-methoxyphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(4-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(naphthalen-1-yl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[2-(3,5-dimethyl-1,2-oxazol-4-yl)ethyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-[[(4-tert-butylphenyl)methyl]sulfanyl]-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R-3-carboxy-3-[(3,4-dimethoxyphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-(cyclohexylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-([[3-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,3-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,6-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2-phenylethyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,4-dimethoxyphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,4-dimethylphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3-phenylpropyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(4-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-1-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]butanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(2,4,6-trimethylphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(2,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(2-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(3,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(3-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(4-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(4-methoxyphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(4-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(naphthalen-1-yl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[2-(3,5-dimethyl-1,2-oxazol-4-yl)ethyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-[[(4-tert-butylphenyl)methyl]sulfanyl]-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[3-[(naphthalen-2-yl)sulfanyl]butanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-[(7S)-7-[[(benzyloxy)carbonyl]amino]-8-([(2S)-3-(1H-indol-3-yl)-1-oxo-1-[(propan-2-yl)amino]propan-2-yl]amino)-8-oxooctanoyl]-beta-alanine
-
N-[(benzyloxy)carbonyl]-5-[2-(4-carboxybutanoyl)hydrazinyl]-L-norvalyl-N-propan-2-yl-L-tryptophanamide
-
N-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-threonyl-L-threonyl-L-alpha-aspartyl-L-serylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-threonyl-L-threonyl-L-alpha-aspartyl-L-serylglycyl-L-valyl-L-leucyl-N6-[3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N2-(benzenesulfonyl)-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-L-tryptophanamide
-
N2-(benzylcarbamoyl)-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-L-tryptophanamide
-
N2-benzoyl-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxy-2,2-difluorobutanoyl)-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-L-tryptophyl-L-aspartamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-L-tryptophyl-L-phenylalaninamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-L-tyrosinamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-N-propan-2-yl-D-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-N-propan-2-yl-L-alaninamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-N-propan-2-yl-L-prolinamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-N-propan-2-yl-L-tryptophanamide
enzyme binding structure, crystal structure analysis
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-N-[(2S)-1,4-diamino-1-oxobutan-2-yl]-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-ethanethioyl-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(2-carboxyethoxy)carbonyl]-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-N-adamantan-1-yl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-N-cyclopropyl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-N-propan-2-yl-L-tryptophanamide
enzyme binding structure, crystal structure analysis
N2-[(benzyloxy)carbonyl]-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-N-[(2S)-1-methoxy-3-phenylpropan-2-yl]-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(2-carboxyethyl)carbamoyl]-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(3R)-4-carboxy-3-methylbutanoyl]-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(3S)-4-carboxy-3-methylbutanoyl]-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(carboxymethyl)carbamothioyl]-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(3-fluorobenzene-1-sulfonyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(3-fluorobenzene-1-sulfonyl)-L-lysyl-N-cyclobutyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(3-fluorobenzene-1-sulfonyl)-L-lysyl-N-cyclopentyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(3-fluorobenzene-1-sulfonyl)-L-lysyl-N-cyclopropyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(3-phenylpropanoyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(4-methoxybenzene-1-sulfonyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(4-nitrobenzene-1-sulfonyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(naphthalene-2-sulfonyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(phenylacetyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(phenylcarbamoyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(quinoline-8-sulfonyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-[4-(trifluoromethyl)benzene-1-sulfonyl]-L-lysyl-L-tryptophanamide
-
N6-[N-[(benzyloxy)carbonyl]-L-gamma-glutamyl]-N2-[(benzyloxy)carbonyl]-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
4-[5-[2-cyano-3-(4-cyano-3-fluoroanilino)-3-oxopropyl]furan-2-yl]benzoic acid
competitive inhibitor
4-[5-[2-cyano-3-(4-cyano-3-fluoroanilino)-3-oxopropyl]furan-2-yl]benzoic acid
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
nicotinamide
nicotinamide inhibition of Sirt5-dependent deacetylation features weak substrate-dependence but requires high, nonphysiological nicotinamide concentrations. The insensitivity of Sirt5 to physiological nicotinamide concentrations is due to a lack of non-competitive inhibition via base exchange, and the inhibition observed at very high nicotinamide concentrations is likely caused by competition with NAD+
suramin
suramin binds into the NAD+-, the product-, and the substrate-binding site
additional information
the acyl-substrate specificity of SIRT5 is adapted to selectively inhibit this isozyme. Synthesis and evaluation of mechanism-based inhibitors of SIRT5, structure-activity relationship, overview
-
additional information
-
the acyl-substrate specificity of SIRT5 is adapted to selectively inhibit this isozyme. Synthesis and evaluation of mechanism-based inhibitors of SIRT5, structure-activity relationship, overview
-
additional information
H3K9TAc and sirtinol show no inhibnition at 0.1 mM
-
additional information
not inhibited by EX527 (i.e. 6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide)
-
additional information
-
not inhibited by EX527 (i.e. 6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide)
-
additional information
the acyl-substrate specificity of SIRT5 is adapted to selectively inhibit this isozyme. Synthesis and evaluation of mechanism-based inhibitors of SIRT5, structure-activity relationship, overview
-
additional information
-
the acyl-substrate specificity of SIRT5 is adapted to selectively inhibit this isozyme. Synthesis and evaluation of mechanism-based inhibitors of SIRT5, structure-activity relationship, overview
-
additional information
no inhibition by (2E)-4,4-dihydroxy-N-[4-[(5-methyl-1,2-oxazol-3-yl)sulfamoyl]phenyl]but-2-enamide; structure-based discovery of selective small-molecul sirtuin 5 inhibitors. Synthesis of (E)-2-cyano-N-phenyl-3-(5-phenylfuran-2-yl)acrylamide derivatives/analogues, docking study, structure-activity relationship analyses, overview. No inhibition by 14 at 0.1 mM
-
additional information
-
no inhibition by (2E)-4,4-dihydroxy-N-[4-[(5-methyl-1,2-oxazol-3-yl)sulfamoyl]phenyl]but-2-enamide; structure-based discovery of selective small-molecul sirtuin 5 inhibitors. Synthesis of (E)-2-cyano-N-phenyl-3-(5-phenylfuran-2-yl)acrylamide derivatives/analogues, docking study, structure-activity relationship analyses, overview. No inhibition by 14 at 0.1 mM
-
additional information
SIRT can be targeted by small molecules, structure-activity relationship study leading to identification of SIRT5 selective inhibitors that exhibit sub-micromolar potency via a slow, tight-binding mechanism
-
additional information
design and synthesis of 9-substituted norharmane derivatives as potential Sirt5 inhibitors, molceular docking, overview
-
additional information
analysis of potent and selective inhibitors of human sirtuin 5, screening and synthesis of 3-arylthiosuccinylated and 3-benzylthiosuccinylated peptide derivatives yielding Sirt5 inhibitors with low-nanomolar Ki values, overview. Crystal structures of Sirt5/ inhibitor complexes reveal that the compounds bind in to the active site of Sirt5. Molecular docking study, computational analysis
-
additional information
-
analysis of potent and selective inhibitors of human sirtuin 5, screening and synthesis of 3-arylthiosuccinylated and 3-benzylthiosuccinylated peptide derivatives yielding Sirt5 inhibitors with low-nanomolar Ki values, overview. Crystal structures of Sirt5/ inhibitor complexes reveal that the compounds bind in to the active site of Sirt5. Molecular docking study, computational analysis
-
additional information
SIRT can be targeted by small molecules, structure-activity relationship study leading to identification of SIRT5 selective inhibitors that exhibited sub-micromolar potency via a slow, tight-binding mechanism
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
resveratrol
0.2 mM resveratrol can stimulate the Sirt5 deacetylase activity against the fluorophore-modified peptide substrate Fluor-de-Lys
cardiolipin
SIRT5 electrostatically binds to cardiolipin, an N-terminal amphipathic helix mediates SIRT5 binding to cardiolipin, cardiolipin activates desuccinylation of membrane proteins
cardiolipin
SIRT5 electrostatically binds to cardiolipin, an N-terminal amphipathic helix mediates SIRT5 binding to cardiolipin, cardiolipin activates desuccinylation of membrane proteins
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08018
[histone H2A]-N6-succinyl-L-lysine95
pH 7.5, 37°C, recombinant enzyme
-
0.10228
[histone H2A]-N6-succinyl-L-lysine9_(4-15)-A10G peptide
pH 7.5, 37°C, recombinant enzyme
-
0.06173
[histone H2B]-N6-succinyl-L-lysine116
pH 7.5, 37°C, recombinant enzyme
-
0.08777
[histone H2B]-N6-succinyl-L-lysine120
pH 7.5, 37°C, recombinant enzyme
-
0.09973
[histone H2B]-N6-succinyl-L-lysine34
pH 7.5, 37°C, recombinant enzyme
-
0.086
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.06051
[histone H3]-N6-succinyl-L-lysine122
pH 7.5, 37°C, recombinant enzyme
-
0.09551
[histone H3]-N6-succinyl-L-lysine14
pH 7.5, 37°C, recombinant enzyme
-
0.10442
[histone H3]-N6-succinyl-L-lysine14_(9-20)-A15G peptide
pH 7.5, 37°C, recombinant enzyme
-
0.17932
[histone H3]-N6-succinyl-L-lysine56
pH 7.5, 37°C, recombinant enzyme
-
0.08489
[histone H3]-N6-succinyl-L-lysine79
pH 7.5, 37°C, recombinant enzyme
-
0.07717
[histone H3]-N6-succinyl-L-lysine9
pH 7.5, 37°C, recombinant enzyme
-
0.10072
[histone H4]-N6-succinyl-L-lysine12
pH 7.5, 37°C, recombinant enzyme
-
0.13153
[histone H4]-N6-succinyl-L-lysine31
pH 7.5, 37°C, recombinant enzyme
-
0.06583
[histone H4]-N6-succinyl-L-lysine31_(26-37)-P32A peptide
pH 7.5, 37°C, recombinant enzyme
-
0.08268
[histone H4]-N6-succinyl-L-lysine77
pH 7.5, 37°C, recombinant enzyme
-
0.10178
[histone H4]-N6-succinyl-L-lysine91
pH 7.5, 37°C, recombinant enzyme
-
0.72
[protein]-N6-acetyl-L-lysine
mutant enzyme Y102A, at 8.0 pH and 25°C
0.069
NAD+
wild type enzyme, with [protein]-N6-succinyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
0.15
NAD+
cosubstrate: Ac-(N6-succinyl)Lys-7-amido-4-methylcoumarin, pH 8.0, 37°C
0.321
NAD+
mutant enzyme Y102A, with [protein]-N6-succinyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
0.609
NAD+
mutant enzyme R105I, with [protein]-N6-acetyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
1.194
NAD+
mutant enzyme Y102A/R105I, with [protein]-N6-acetyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
1.605
NAD+
mutant enzyme Y102A, with [protein]-N6-acetyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
0.0147
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme Y92F
-
0.0151
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.02
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme R95M
-
0.29
[protein]-N6-succinyl-L-lysine
wild type enzyme, at 8.0 pH and 25°C
0.388
[protein]-N6-succinyl-L-lysine
mutant enzyme Y102A/R105I, at 8.0 pH and 25°C
1.658
[protein]-N6-succinyl-L-lysine
mutant enzyme R105I, at 8.0 pH and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.219
[histone H2A]-N6-succinyl-L-lysine95
pH 7.5, 37°C, recombinant enzyme
-
0.199
[histone H2A]-N6-succinyl-L-lysine9_(4-15)-A10G peptide
pH 7.5, 37°C, recombinant enzyme
-
0.297
[histone H2B]-N6-succinyl-L-lysine116
pH 7.5, 37°C, recombinant enzyme
-
0.279
[histone H2B]-N6-succinyl-L-lysine120
pH 7.5, 37°C, recombinant enzyme
-
0.314
[histone H2B]-N6-succinyl-L-lysine34
pH 7.5, 37°C, recombinant enzyme
-
0.242
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.178
[histone H3]-N6-succinyl-L-lysine122
pH 7.5, 37°C, recombinant enzyme
-
0.2
[histone H3]-N6-succinyl-L-lysine14
pH 7.5, 37°C, recombinant enzyme
-
0.186
[histone H3]-N6-succinyl-L-lysine14_(9-20)-A15G peptide
pH 7.5, 37°C, recombinant enzyme
-
0.512
[histone H3]-N6-succinyl-L-lysine56
pH 7.5, 37°C, recombinant enzyme
-
0.213
[histone H3]-N6-succinyl-L-lysine79
pH 7.5, 37°C, recombinant enzyme
-
0.336
[histone H3]-N6-succinyl-L-lysine9
pH 7.5, 37°C, recombinant enzyme
-
0.202
[histone H4]-N6-succinyl-L-lysine12
pH 7.5, 37°C, recombinant enzyme
-
0.224
[histone H4]-N6-succinyl-L-lysine31
pH 7.5, 37°C, recombinant enzyme
-
0.189
[histone H4]-N6-succinyl-L-lysine31_(26-37)-P32A peptide
pH 7.5, 37°C, recombinant enzyme
-
0.208
[histone H4]-N6-succinyl-L-lysine77
pH 7.5, 37°C, recombinant enzyme
-
0.294
[histone H4]-N6-succinyl-L-lysine91
pH 7.5, 37°C, recombinant enzyme
-
0.000066
[protein]-N6-acetyl-L-lysine
mutant enzyme Y102A, at 8.0 pH and 25°C
0.000026
NAD+
mutant enzyme Y102A/R105I, with [protein]-N6-acetyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
0.000122
NAD+
mutant enzyme R105I, with [protein]-N6-acetyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
0.000274
NAD+
mutant enzyme Y102A, with [protein]-N6-succinyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
0.04
NAD+
wild type enzyme, with [protein]-N6-succinyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
0.052
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme Y92F
-
0.059
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme R95M
-
0.135
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.000026
[protein]-N6-succinyl-L-lysine
mutant enzyme Y102A/R105I, at 8.0 pH and 25°C
0.000274
[protein]-N6-succinyl-L-lysine
mutant enzyme R105I, at 8.0 pH and 25°C
0.04
[protein]-N6-succinyl-L-lysine
wild type enzyme, at 8.0 pH and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.73
[histone H2A]-N6-succinyl-L-lysine95
pH 7.5, 37°C, recombinant enzyme
-
1.95
[histone H2A]-N6-succinyl-L-lysine9_(4-15)-A10G peptide
pH 7.5, 37°C, recombinant enzyme
-
4.81
[histone H2B]-N6-succinyl-L-lysine116
pH 7.5, 37°C, recombinant enzyme
-
3.18
[histone H2B]-N6-succinyl-L-lysine120
pH 7.5, 37°C, recombinant enzyme
-
3.15
[histone H2B]-N6-succinyl-L-lysine34
pH 7.5, 37°C, recombinant enzyme
-
2.94
[histone H3]-N6-succinyl-L-lysine122
pH 7.5, 37°C, recombinant enzyme
-
2.09
[histone H3]-N6-succinyl-L-lysine14
pH 7.5, 37°C, recombinant enzyme
-
1.78
[histone H3]-N6-succinyl-L-lysine14_(9-20)-A15G peptide
pH 7.5, 37°C, recombinant enzyme
-
2.86
[histone H3]-N6-succinyl-L-lysine56
pH 7.5, 37°C, recombinant enzyme
-
2.51
[histone H3]-N6-succinyl-L-lysine79
pH 7.5, 37°C, recombinant enzyme
-
4.35
[histone H3]-N6-succinyl-L-lysine9
pH 7.5, 37°C, recombinant enzyme
-
2.01
[histone H4]-N6-succinyl-L-lysine12
pH 7.5, 37°C, recombinant enzyme
-
1.7
[histone H4]-N6-succinyl-L-lysine31
pH 7.5, 37°C, recombinant enzyme
-
2.87
[histone H4]-N6-succinyl-L-lysine31_(26-37)-P32A peptide
pH 7.5, 37°C, recombinant enzyme
-
2.52
[histone H4]-N6-succinyl-L-lysine77
pH 7.5, 37°C, recombinant enzyme
-
2.89
[histone H4]-N6-succinyl-L-lysine91
pH 7.5, 37°C, recombinant enzyme
-
3
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme R95M
-
3.5
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme Y92F
-
8.9
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.022
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme R95M
-
0.067
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme Y92F
-
2.8
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0043
benzoyl-GVL(N6-(3-methyl-3-phenyl)succinyl)KEYGV-amide
pH 7.8, 37°C
0.0381
benzoyl-GVL(N6-(N-benzyloxycarbonyl-L-aspartyl))KEYGV-amide
pH 7.8, 37°C
0.0249
benzoyl-GVL(N6-(N-phthaloyl-DL-gamma-glutamyl))KEYGV-amide
pH 7.8, 37°C
0.0043
N-benzylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-phenylbutanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
pH 7.8, 37°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07256
(2S)-2-[(naphthalen-2-yl)sulfanyl]-4-oxo-4-[(3-phenylpropyl)amino]butanoic acid
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.124
(2S)-4-(benzylamino)-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.09
(2S)-4-[3-(methylcarbamoyl)anilino]-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.074
(2S)-4-[[(5S)-5-acetamido-6-amino-6-oxohexyl]amino]-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0195
(3E)-3-[(3,5-dibromo-4-hydroxyphenyl)methylidene]-5-iodo-1,3-dihydro-2H-indol-2-one
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0559
(5E)-1-ethyl-5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.027
(5E)-5-(1H-indol-3-ylmethylidene)-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0673
(5E)-5-[4-(benzyloxy)benzylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0129
(5E)-5-[4-(benzyloxy)benzylidene]-1-ethyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0178
(5E)-5-[4-(benzyloxy)benzylidene]-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0023
(5E)-5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-1-(prop-2-en-1-yl)-2-sulfanylidene-1,3-diazinane-4,6-dione
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0023
(5E)-5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.001
(N6-thiosuccinyl)KSTGGKA
Homo sapiens
pH and temperature not specified in the publication
0.0001
1,8-dihydroxyanthracen-9(10H)-one
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0056
4-[5-[2-cyano-3-(4-cyano-3-fluoroanilino)-3-oxopropyl]furan-2-yl]benzoic acid
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0465
5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.03
5-(biphenyl-4-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0166
5-[(1-benzyl-1H-indol-3-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0224
5-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0126
5-[4-(benzyloxy)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0394
5-[4-(propan-2-yl)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0124
5-[4-[(2-chlorobenzyl)oxy]-3-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0062
5-[4-[(4-bromobenzyl)oxy]benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0126
5-[[4-(benzyloxy)phenyl]methylidene]-2-sulfanylidene-1,3-diazinane-4,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0036
5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.04
Ac-AR(N6-thiosuccinyl)KST-NH2
Homo sapiens
pH and temperature not specified in the publication
0.025
Ac-RR(N6-thiosuccinyl)KRR-NH2
Homo sapiens
pH and temperature not specified in the publication
0.03
AR(N6-thiosuccinyl)KST
Homo sapiens
pH and temperature not specified in the publication
0.001
KQTAR(N6-thiosuccinyl)K
Homo sapiens
pH and temperature not specified in the publication
0.005
KQTAR(N6-thiosuccinyl)KSTGGKA
Homo sapiens
pH and temperature not specified in the publication
0.005
L-lysyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-N6-(3-carboxypropanethioyl)-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanine
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0075
N-([4-[(3S,6S,9S)-9-acetamido-27-[[(2S,3R)-1-amino-3-hydroxy-1-oxobutan-2-yl]carbamoyl]-6-(3-carbamimidamidopropyl)-2,5,8,14,21-pentaoxo-1,4,7,13,22-pentaazacycloheptacosan-3-yl]butyl]carbamothioyl)-beta-alanine
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00035
N-acetyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alaninamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001075
N-acetyl-L-leucyl-N6-[3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alaninamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.022803
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-[[2-(pyrazin-2-yl)ethyl]sulfanyl]propanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.006966
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-[[2-(pyridin-2-yl)ethyl]sulfanyl]propanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.013244
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-[[2-(pyridin-4-yl)ethyl]sulfanyl]propanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001122
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-4-phenylbutanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000644
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.014
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-(cyclohexylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001799
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001148
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-([[3-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.002203
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.003388
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2,3-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.002013
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.012503
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2,6-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.003097
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000592
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2-phenylethyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001607
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001259
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3,4-dimethylphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000647
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001384
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.002061
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3-phenylpropyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001614
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(4-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.002196
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(naphthalen-1-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00009
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]butanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00181
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000631
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(2,4,6-trimethylphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000432
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(2,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000352
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(2-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00078
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(3,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.002673
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(3-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001021
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(4-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001112
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(4-methoxyphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0004027
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(4-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000207
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(naphthalen-1-yl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.018493
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[2-(3,5-dimethyl-1,2-oxazol-4-yl)ethyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001236
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-[[(4-tert-butylphenyl)methyl]sulfanyl]-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.009078
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R-3-carboxy-3-[(3,4-dimethoxyphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000336
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.004
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-(cyclohexylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000274
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001125
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-([[3-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000804
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000715
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,3-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000177
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000295 - 0.001977
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
0.000577
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,6-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000857
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.002742
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2-phenylethyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000046
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000326
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,4-dimethoxyphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000046
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,4-dimethylphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000086
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00012
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00113
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3-phenylpropyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000102
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(4-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000095
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-1-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000059
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]butanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00003
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0052
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(2,4,6-trimethylphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000543
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(2,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000533
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(2-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00074
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(3,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00271
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(3-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000893
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(4-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001047
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(4-methoxyphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.003732
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(4-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000015
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(naphthalen-1-yl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00875
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[2-(3,5-dimethyl-1,2-oxazol-4-yl)ethyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000793
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-[[(4-tert-butylphenyl)methyl]sulfanyl]-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.04
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[3-[(naphthalen-2-yl)sulfanyl]butanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.04
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0000191
N-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-threonyl-L-threonyl-L-alpha-aspartyl-L-serylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0000911
N-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-threonyl-L-threonyl-L-alpha-aspartyl-L-serylglycyl-L-valyl-L-leucyl-N6-[3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.01572
(2S)-4-(butylamino)-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.154
(2S)-4-(butylamino)-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0195
3-(3,5-dibromo-4-hydroxybenzyliden)-5-iodo-1,3-dihydroindol-2-one
Homo sapiens
pH 7.5, temperature not specified in the publication, substrate: SKEYFS-(succinylLys)-QK
0.097
3-(3,5-dibromo-4-hydroxybenzyliden)-5-iodo-1,3-dihydroindol-2-one
Homo sapiens
pH 7.5, temperature not specified in the publication, substrate: FKRGVL-(acetylLys)-EYGVKV
0.0111
Isonicotinamide
Homo sapiens
wild type enzyme, with 0.05 mM NAD+, at 8.0 pH and 25°C
0.000295
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001977
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.021
nicotinamide
Homo sapiens
pH 7.8, 37°C, substrate: benzoyl-RGVL(succK)EYGV-amide
0.0142
suramin
Homo sapiens
pH 7.5, temperature not specified in the publication, substrate: acetylated peptide derived from carbamoylphosphate synthetase 1 (CPS1)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Escherichia coli W3110 / ATCC 27325
strain W3110 is a K12 derivative that is wild-type for chemotaxis
-
-
brenda
strain W3110 is a K12 derivative that is wild-type for chemotaxis
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-
brenda
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728857, 728962, 729138, 729372, 729547, 729801, 729885, 729993, 730024, 730161, 730205, 730245, 730474, 730706, 730713, 730922, 730964, 730974, 731010
SwissProt
brenda
-
738843, 739445, 755788, 755970, 756010, 756427, 756522, 756680, 757175, 757350, 757400, 757590, 758247
SwissProt
brenda
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SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
in the cerebellar cortex, SIRT5 can be found in Purkinje cells, and is mainly distributed in the cytoplasm, but is not markedly expressed in the molecular layer or granular layer cells
brenda
SIRT5 and SIRT1/2 have opposite expression patterns and functions in macrophages, overview
brenda
SIRT5 is overexpressed in human non-small cell lung cancer cells, high expression of SIRT5 predicts poor survival
brenda
additional information
SIRT5 expression is observed to localize strictly to the periportal hepatocytes
brenda
additional information
SIRT5 displays broad tissue distribution, with highest levels in brain, heart, liver, kidney, muscle, and testis
brenda
additional information
sirtuin 5 (SIRT5) is upregulated in patients with type 2 diabetes and in pancreatic beta cell lines
brenda
additional information
-
sirtuin 5 (SIRT5) is upregulated in patients with type 2 diabetes and in pancreatic beta cell lines
brenda
additional information
the SIRT5 gene is widely expressed, but expression patterns of different isoforms vary in tissues, expression analysis, overview
brenda
additional information
-
the SIRT5 gene is widely expressed, but expression patterns of different isoforms vary in tissues, expression analysis, overview
brenda
additional information
SIRT5 displays broad tissue distribution, with highest levels in brain, heart, liver, kidney, muscle, and testis
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
SIRT5 isoforms (i.e., SIRT5iso1 and SIRT5iso2) are encoded by the human SIRT5 gene. Their C-termini slightly differ from each other. Although both isoforms contain cleavable mitochondrial targeting signals at their N-termini,it is found that the cleaved SIRT5iso2 is localized mainly in mitochondria, whereas the cleaved SIRT5iso1 is localized in both mitochondria and cytoplasm. The cytoplasmic localization of cleaved SIRT5iso1 is dependent on the SIRT5iso1-specific C-terminus
brenda
SIRT5 isozyme 4 is mainly localized in the cytoplasm
brenda
mainly distributed in the cytoplasm of Purkinje cells
brenda
SIRT5 is targeted to protein complexes on the inner mitochondrial membrane via affinity for cardiolipin
brenda
SIRT5 is targeted to protein complexes on the inner mitochondrial membrane via affinity for cardiolipin
brenda
Sirt5 can be translocated into the mitochondrial intermembrane space, but also into the matrix
brenda
SIRT5 isoforms (i.e., SIRT5iso1 and SIRT5iso2) are encoded by the human SIRT5 gene. Their C-termini slightly differ from each other. Although both isoforms contain cleavable mitochondrial targeting signals at their N-termini, it is found that the cleaved SIRT5iso2 is localized mainly in mitochondria, whereas the cleaved SIRT5iso1 is localized in both mitochondria and cytoplasm. The C-terminus of SIRT5iso2, which is rich in hydrophobic amino acid residues, functions as a mitochondrial membrane insertion signal
brenda
SIRT5 isozymes 1, 2 and 3 are mitochondria-localized. The full-length SIRT5 protein (SIRT5iso1) contains the N-terminal 36 amino acid mitochondrial localization signal (MLS) peptide
brenda
SIRT5 is present both mitochondrially and extramitochondrially
brenda
a very small amount of SIRT5 is detected in the nuclear fraction
brenda
additional information
although Sirt5 localizes mainly in the mitochondria, a slight amount of Sirt5 is detected in the nuclear fraction
-
brenda
additional information
-
although Sirt5 localizes mainly in the mitochondria, a slight amount of Sirt5 is detected in the nuclear fraction
-
brenda
additional information
SIRT5 is predominantly a mitochondrial matrix protein, but a significant portion of SIRT5 localizes to the cytosol, peroxisomes, and nucleus as well. SIRT5 activity is non-redundant with other sirtuins in mitochondria, and likely elsewhere in the cell as well
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brenda
additional information
SIRT5 is predominantly a mitochondrial matrix protein, but a significant portion of SIRT5 localizes to the cytosol, peroxisomes, and nucleus as well. SIRT5 activity is non-redundant with other sirtuins in mitochondria, and likely elsewhere in the cell as well
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism